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  Membrane targeting of the spir·formin actin nucleator complex requires a sequential handshake of polar interactions.

Tittel, J., Welz, T., Czogalla, A., Dietrich, S., Samol-Wolf, A., Schulte, M., et al. (2015). Membrane targeting of the spir·formin actin nucleator complex requires a sequential handshake of polar interactions. The Journal of biological chemistry, 290(10), 6428-6444. doi:10.1074/jbc.M114.602672.

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 Creators:
Tittel, Janine1, Author           
Welz, Tobias2, Author
Czogalla, Aleksander2, Author
Dietrich, Susanne2, Author
Samol-Wolf, Annette2, Author
Schulte, Markos2, Author
Schwille, Petra1, Author           
Weidemann, Thomas1, Author           
Kerkhoff, Eugen2, Author
Affiliations:
1Schwille, Petra / Cellular and Molecular Biophysics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565169              
2external, ou_persistent22              

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 Abstract: Spir and formin (FMN)-type actin nucleators initiate actin polymerization at vesicular membranes necessary for long range vesicular transport processes. Here we studied in detail the membrane binding properties and protein/protein interactions that govern the assembly of the membrane-associated Spir·FMN complex. Using biomimetic membrane models we show that binding of the C-terminal Spir-2 FYVE-type zinc finger involves both the presence of negatively charged lipids and hydrophobic contributions from the turret loop that intrudes the lipid bilayer. In solution, we uncovered a yet unknown intramolecular interaction between the Spir-2 FYVE-type domain and the N-terminal kinase non-catalytic C-lobe domain (KIND) that could not be detected in the membrane-bound state. Interestingly, we found that the intramolecular Spir-2 FYVE/KIND and the trans-regulatory Fmn-2-FSI/Spir-2-KIND interactions are competitive. We therefore characterized co-expressed Spir-2 and Fmn-2 fluorescent protein fusions in living cells by fluorescence cross-correlation spectroscopy. The data corroborate a model according to which Spir-2 exists in two different states, a cytosolic monomeric conformation and a membrane-bound state in which the KIND domain is released and accessible for subsequent Fmn-2 recruitment. This sequence of interactions mechanistically couples membrane binding of Spir to the recruitment of FMN, a pivotal step for initiating actin nucleation at vesicular membranes.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 17
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 25564607
DOI: 10.1074/jbc.M114.602672
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Title: The Journal of biological chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 290 (10) Sequence Number: - Start / End Page: 6428 - 6444 Identifier: -